ID A0A4Z1IU99_9HELO Unreviewed; 522 AA.
AC A0A4Z1IU99;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=BELL_1027g00010 {ECO:0000313|EMBL:TGO64915.1};
OS Botrytis elliptica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=278938 {ECO:0000313|EMBL:TGO64915.1, ECO:0000313|Proteomes:UP000297229};
RN [1] {ECO:0000313|EMBL:TGO64915.1, ECO:0000313|Proteomes:UP000297229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Be9601 {ECO:0000313|EMBL:TGO64915.1,
RC ECO:0000313|Proteomes:UP000297229};
RA Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA Valdes J.H., Van Kan J.A.L.;
RT "Comparative genomics of Botrytis spp.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TGO64915.1}.
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DR EMBL; PQXM01001025; TGO64915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z1IU99; -.
DR STRING; 278938.A0A4Z1IU99; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000297229; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR055916; DUF7493.
DR InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF31; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF24321; DUF7493; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000297229};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..290
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57059 MW; E9D3D91A017075BE CRC64;
MATSPTSSNS IPPSGQTASS GSAGQFDIDN TLFVSKDVSL SLSPESLVIK GAETAKKPEK
GAKSAGARRS VTLDASAYSE PVGASTLRAI PLRQILWAEI TETELIINYA KEISKTVLQP
AVLKYVIEEE RDRVEAWVSR LKDRAYGKSQ QQKRVKVIIN PKSGKGQSEK IYAKDVAPIF
DAAHLSIDVT VTKASREATD IVEKLDIEAF DVIICCSGDG LPFEVFNGLG KRKDAKRALS
KMAIAHIPCG SGNGLHCSLH GNIRSTSIAA LSIVKGIRTP LDLISVTQGE ERHLSFLSQA
LGIVAEFDLG TEHLRWMGGT RFVYGFVMKS LQKKIFPCDI AVKVVADDKE DIKRRYRETM
EIGSTSEELL RENGSLEGGL PKLKYGNSSD PLPQGWEVEQ HDNLGSFYCG NMSWMGADVD
YFPAALPNDG CMDMVTIDYS NLSRLQALQL MPAVESGKFF GLPYVNYRKV EAYRITPKNQ
SDGYISIDGE RVPFGPFQAE VHRGLGTVLS VSGYRYETPG PK
//